Research workbench
Open conformation of francisella tularensis clpp at 1.7 a
Analyse Open conformation of francisella tularensis clpp at 1.7 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G1S
- Type
- protein
- Length
- 3,966 residues
- Chains
- 21
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit
- EC
- 3.4.21.92
- UniProt
- A0A0E2ZNT9
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 16 distinct chains · 45% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 188 | 45% helix, 23% strand | A0A0E2ZNT9 |
| B | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 183 | 46% helix, 21% strand | A0A0E2ZNT9 |
| C, E | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 189 | 44% helix, 21% strand | A0A0E2ZNT9 |
| D | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 187 | 45% helix, 22% strand | A0A0E2ZNT9 |
| F, T | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 191 | 44% helix, 25% strand | A0A0E2ZNT9 |
| G, K, N, U | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 193 | 44% helix, 20% strand | A0A0E2ZNT9 |
| H | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 190 | 44% helix, 27% strand | A0A0E2ZNT9 |
| I | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 184 | 46% helix, 25% strand | A0A0E2ZNT9 |
| J | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 188 | 45% helix, 24% strand | A0A0E2ZNT9 |
| L | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 188 | 45% helix, 25% strand | A0A0E2ZNT9 |
| M | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 192 | 43% helix, 28% strand | A0A0E2ZNT9 |
| O | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 189 | 44% helix, 26% strand | A0A0E2ZNT9 |
| P | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 181 | 47% helix, 25% strand | A0A0E2ZNT9 |
| Q | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 188 | 45% helix, 25% strand | A0A0E2ZNT9 |
| R | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 186 | 45% helix, 24% strand | A0A0E2ZNT9 |
| S | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 190 | 44% helix, 25% strand | A0A0E2ZNT9 |
Ligands and binding sites
- ACT · Acetate ion · additive · 21 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U
- MRD · (4R)-2-methylpentane-2,4-diol · additive · 18 copies · chains A, B, C, D, G, I, J, K, L, M, N, O, P, Q, S, T, U
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 14 copies · chains B, C, D, E, F, G, I, J, L, M, H, N, S, T, U
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 849 | 0.81 | 0.84 | 88 | MPD |
| 2 | 1029 | 0.76 | 0.78 | 85 | empty |
| 3 | 898 | 0.74 | 0.78 | 108 | ACT |
| 4 | 668 | 0.74 | 0.80 | 87 | ACT |
| 5 | 464 | 0.73 | 0.82 | 77 | ACT |
Interfaces
62 interfaces between chains.
- F–G · 2166 Ų buried · 33 hydrogen bonds · protein-protein
- M–N · 2157 Ų buried · 37 hydrogen bonds · protein-protein
- T–U · 2127 Ų buried · 35 hydrogen bonds · protein-protein
- J–K · 2069 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 1978 Ų buried · 28 hydrogen bonds · protein-protein
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A0E2ZNT9
- Elsewhere: RCSB PDB 5G1S · PDBe 5G1S · UniProt A0A0E2ZNT9
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